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P11977 (PGK_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglycerate kinase

EC=2.7.2.3
Gene names
Name:pgkA
Synonyms:pgk
ORF Names:AN1246
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. HAMAP-Rule MF_00145

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00145

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00145.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from direct assay PubMed 20797444. Source: ASPGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglycerate kinase activity

Inferred from mutant phenotype PubMed 8431952. Source: ASPGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_0000145880

Regions

Nucleotide binding375 – 3784ATP By similarity
Region24 – 263Substrate binding By similarity
Region66 – 694Substrate binding By similarity

Sites

Binding site421Substrate By similarity
Binding site1251Substrate By similarity
Binding site1731Substrate By similarity
Binding site2221ATP By similarity
Binding site3151ATP; via carbonyl oxygen By similarity
Binding site3461ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P11977 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: CBC948382ECE212D

FASTA42144,909
        10         20         30         40         50         60 
MSLTSKLSIT DVDLKDKRVL IRVDFNVPLD KNDNTTITNP QRIVGALPTI KYAIDNGAKA 

        70         80         90        100        110        120 
VILMSHLGRP DGKKNPKYSL KPVVPKLKEL LGRDVIFTED CVGPEVEETV NKASGGQVIL 

       130        140        150        160        170        180 
LENLRFHAEE EGSSKDADGN KVKADKDAVA QFRKGLTALG DIYINDAFGT AHRAHSSMVG 

       190        200        210        220        230        240 
VDLPQKASGF LVKKELEYFA KALEEPQRPF LAILGGSKVS DKIQLIDNLL PKVNSLIITG 

       250        260        270        280        290        300 
GMAFTFKKTL ENVKIGSSLF DEAGSKIVGN IIEKAKKHNV KVVLPVDYVT ADKFAADAKT 

       310        320        330        340        350        360 
GYATDEQGIP DGYMGLDVGE KSVESYKQTI AESKTILWNG PPGVFEMEPF AKATKATLDA 

       370        380        390        400        410        420 
AVAAVQNGAT VIIGGGDTAT VAAKYGAEDK ISHVSTGGGA SLELLEGKEL PGVAALSEKS 


K 

« Hide

References

« Hide 'large scale' references
[1]"Transcription and processing signals in the 3-phosphoglycerate kinase (PGK) gene from Aspergillus nidulans."
Clements J.M., Roberts C.F.
Gene 44:97-105(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27549 Genomic DNA. Translation: AAA33318.1.
AACD01000017 Genomic DNA. Translation: EAA65839.1.
BN001308 Genomic DNA. Translation: CBF87861.1.
PIRA24830.
RefSeqXP_658850.1. XM_653758.1.

3D structure databases

ProteinModelPortalP11977.
SMRP11977. Positions 2-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00001377.

Proteomic databases

PRIDEP11977.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00001377; CADANIAP00001377; CADANIAG00001377.
GeneID2877015.
KEGGani:AN1246.2.

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAGLDCGEK.
OrthoDBEOG71K6D7.

Family and domain databases

Gene3D3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPMF_00145. Phosphoglyc_kinase.
InterProIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERPTHR11406. PTHR11406. 1 hit.
PfamPF00162. PGK. 1 hit.
[Graphical view]
PIRSFPIRSF000724. Pgk. 1 hit.
PRINTSPR00477. PHGLYCKINASE.
SUPFAMSSF53748. SSF53748. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGK_EMENI
AccessionPrimary (citable) accession number: P11977
Secondary accession number(s): C8VSJ5, Q5BDY4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families